If you had to mutate a Phe residue that occurs in a helix within a protein,...
If you had to mutate a Phe residue that occurs in a helix within a protein, but wanted to disturb the structure of the globular protein as little as possible, what amino acid might be a good choice, and why?
Homework Answers
To replace mutated Phe with another amino acid without disturbing the globular protein structure as little as possible the good choice would be Tyr (Tyrosine). Phe or Phenylalanine is closely related to Tyr or tyrosine on the basis of their structural similarity. Phe is an essential amino acid which means it should be present in our diet as our body is not able to synthesize it. Whereas tyrosine is produced in our body by the hydroxylation of phenylalanine and the diet rich in tyrosine is able to reduce our bodily need for phenylalanine.
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If you had to mutate a Phe residue that occurs in a helix within
a protein,...
Please answer thoroughly, will rate thumbs up. thanks Q1. Consider the following protein sequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg-Leu-Lys-Ile-Arg-Phe-Glu. What...
Please answer thoroughly, will rate thumbs up. thanks Q1. Consider the following protein sequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg-Leu-Lys-Ile-Arg-Phe-Glu. What is special about the arrangement of the amino acids in these sequences when incorporated into a Beta sheet? What prediction can you make about how this Beta sheet might be arranged in a cytoplasmic protein. Q2. Consider the following protein sequence as an Alpha-helix: Leu-Lys-Arg-Ile-Val-Asp-Ile-Leu-Ser-Arg-Leu-Phe-Lys-Val. What is special about the arrangement of the amino acids in these sequences when folded into alpha helix?
Question 5 Bio206 Homework 6 Amino Acids and Proteins Organic Chemistry II Due May 6, 2017 1. Which amino acid is least likely to be found in a natural protein? CH20H NHz CHs IV 2. A pentapeptide has...
Question 5
Bio206 Homework 6 Amino Acids and Proteins Organic Chemistry II Due May 6, 2017 1. Which amino acid is least likely to be found in a natural protein? CH20H NHz CHs IV 2. A pentapeptide has the molecular formula: Asp, Glu, His, Phe, Val. Partial hydrolysis of the pentapeptide gives: Val Asp, Glu His, Phe Val, and Asp Glu. What is the amino acid sequence of the pentapeptide? 3. When the pentapeptide below is heated first with 2,4-dinitrofluorobenzene...
1. The following amino acid sequence is observed in an alpha-helical segment of a polypeptide: L D E N I K R N A Q L V E...
1. The following amino acid sequence is observed in an alpha-helical segment of a polypeptide: L D E N I K R N A Q L V E Q Q I R What pattern, if any, seems to characterize this sequence? Explain why this pattern might be occurring in terms of the 3D structure of the protein. 2. Indicate the probable location of the following amino acid residues in a native globular protein. a) Asp b) Phe c) Met d)...
11.Which of the following mutations would most likely to disrupt the structure of an α-helix? Cys...
11.Which of the following mutations would most likely to disrupt the structure of an α-helix? Cys to Ala Lys to Arg Glu to Gly Val to Leu 12.Which amino acid combination is the most preferred to occupy positions 1 and 4 in an α-helix? Glu and Lys Phe and Pro Lys and Arg Asp and Glu 13.If each turn in the standard alpha helix extends 5.4 A and there are 3.6 amino acid residues per turn, how many amino acids...
please answer 4. Secondary structure (a-helix): The image below is of a polypeptide in secondary (2)...
please answer
4. Secondary structure (a-helix): The image below is of a polypeptide in secondary (2) structure level of protein folding. Specifically it is of an a-helix. Use the image on the left to answer the questions a-e below. The image on the right is to help with question "f' only. a. Name the specific bond/interaction indicated by the dotted lines. b. Is this bond/interaction covalent or non-covalent? c. Is this bond/interaction permanent or transient? d. What parts of the...
Consider the following amino acid sequence, found as part of a larger protein: Pro-Gly-Asp-Val-Gln-Phe-Asp-Ile-Arg-Ala-Asp-Gly What kind...
Consider the following amino acid sequence, found as part of a larger protein: Pro-Gly-Asp-Val-Gln-Phe-Asp-Ile-Arg-Ala-Asp-Gly What kind of structure do you expect this peptide segment be a part of? Where on the protein is this likely to occur?
ONLY ANSWER IF YOU KNOW! The reorganization of protein domains often elicits the architectural impetus for...
ONLY ANSWER IF YOU KNOW!
The reorganization of protein domains often elicits the architectural impetus for signal initiation in biological systems. For instance, the MAP kinase, Cdk2, has three Arg residues at positions 50, 126, and 150, and a Thr residue at position 160. If no post- translational modifications occur on any of the four amino acid residues, no interaction occurs. However, if the Thr residue is phosphorylated, structural rearrangement occurs to obtain the conformation shown below. Why does this...
4. A certain protein is known to be embedded within a cell membrane. What type of...
4. A certain protein is known to be embedded within a cell membrane. What type of amino acids would you expect this protein to contain on its surface and why? 5. Structural proteins form the basis for hair and nails and have a high cysteine content. Cysteine side groups (-CH2SH) can react with each other to form disulfide bridge. What type of bonding holds the bridge together? Why is this interaction important for the function of structural proteins? Hemoglobin is...
Question 10 (4 points) Although all protein structures are unique, there are common structural building blocks...
Question 10 (4 points) Although all protein structures are unique, there are common structural building blocks that are referred to as regular secondary structures, Some proteins have alpha-helices, some have beta-sheets, and still others have a combination of both. What makes it possible for proteins to have these common structural elements? 12 15 a) the hydrophobic-core interactions. b) hydrogen bonds that form along (alpha helices) or between (beta sheets) polypeptide backbones. c) side-chain interactions d) specific amino acid sequences. 7...
Consider the following amino acids for questions 11-13. Choose the best answers. cysteine serine lysine phenylalanine...
Consider the following amino acids for questions 11-13. Choose the best answers. cysteine serine lysine phenylalanine aspartate Which amino acid's R group has a pKa nearest physiological pH? Which amino acid would you most expect to find in the centre of a folded globular protein? Which amino amino acid can be phosphorylated? The overall charge on the peptide (G-R-A-M-P-S) at pH 12.5 is: -1 -0.5 -1.5 +0.5 1 15. What term best describes the protein secondary structure element drawn below:...
Question 5
Bio206 Homework 6 Amino Acids and Proteins Organic Chemistry II Due May 6, 2017 1. Which amino acid is least likely to be found in a natural protein? CH20H NHz CHs IV 2. A pentapeptide has the molecular formula: Asp, Glu, His, Phe, Val. Partial hydrolysis of the pentapeptide gives: Val Asp, Glu His, Phe Val, and Asp Glu. What is the amino acid sequence of the pentapeptide? 3. When the pentapeptide below is heated first with 2,4-dinitrofluorobenzene...
please answer
4. Secondary structure (a-helix): The image below is of a polypeptide in secondary (2) structure level of protein folding. Specifically it is of an a-helix. Use the image on the left to answer the questions a-e below. The image on the right is to help with question "f' only. a. Name the specific bond/interaction indicated by the dotted lines. b. Is this bond/interaction covalent or non-covalent? c. Is this bond/interaction permanent or transient? d. What parts of the...
ONLY ANSWER IF YOU KNOW!
The reorganization of protein domains often elicits the architectural impetus for signal initiation in biological systems. For instance, the MAP kinase, Cdk2, has three Arg residues at positions 50, 126, and 150, and a Thr residue at position 160. If no post- translational modifications occur on any of the four amino acid residues, no interaction occurs. However, if the Thr residue is phosphorylated, structural rearrangement occurs to obtain the conformation shown below. Why does this...
4. A certain protein is known to be embedded within a cell membrane. What type of amino acids would you expect this protein to contain on its surface and why? 5. Structural proteins form the basis for hair and nails and have a high cysteine content. Cysteine side groups (-CH2SH) can react with each other to form disulfide bridge. What type of bonding holds the bridge together? Why is this interaction important for the function of structural proteins? Hemoglobin is...
Question 10 (4 points) Although all protein structures are unique, there are common structural building blocks that are referred to as regular secondary structures, Some proteins have alpha-helices, some have beta-sheets, and still others have a combination of both. What makes it possible for proteins to have these common structural elements? 12 15 a) the hydrophobic-core interactions. b) hydrogen bonds that form along (alpha helices) or between (beta sheets) polypeptide backbones. c) side-chain interactions d) specific amino acid sequences. 7...
Consider the following amino acids for questions 11-13. Choose the best answers. cysteine serine lysine phenylalanine aspartate Which amino acid's R group has a pKa nearest physiological pH? Which amino acid would you most expect to find in the centre of a folded globular protein? Which amino amino acid can be phosphorylated? The overall charge on the peptide (G-R-A-M-P-S) at pH 12.5 is: -1 -0.5 -1.5 +0.5 1 15. What term best describes the protein secondary structure element drawn below:...
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